A study of a Calpha,beta-didehydroalanine homo-oligopeptide series in the solid-state by 13C cross-polarization magic angle spinning NMR

Katherine A Henzler Wildman; Ayyalusamy Ramamoorthy; Tateaki Wakamiya; Taichi Yoshikawa; Marco Crisma; Claudio Toniolo; Fernando Formaggio

doi:10.1002/psc.551

A study of a Calpha,beta-didehydroalanine homo-oligopeptide series in the solid-state by 13C cross-polarization magic angle spinning NMR

J Pept Sci. 2004 Jun;10(6):336-41. doi: 10.1002/psc.551.

Authors

Katherine A Henzler Wildman¹, Ayyalusamy Ramamoorthy, Tateaki Wakamiya, Taichi Yoshikawa, Marco Crisma, Claudio Toniolo, Fernando Formaggio

Affiliation

¹ Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA.

PMID: 15214438
DOI: 10.1002/psc.551

Abstract

The fully extended peptide conformation (2.0(5)-helix) has been investigated for the first time in the solid-state by 13C cross-polarization magic angle spinning NMR. The compounds examined are members of a terminally protected, homo-oligopeptide series (from monomer through hexamer) based on Calpha,beta-didehydroalanine.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Alanine / chemistry*
Carbon Isotopes
Magnetic Resonance Spectroscopy
Molecular Structure
Oligopeptides / chemical synthesis
Oligopeptides / chemistry*
Protein Conformation

Substances

Carbon Isotopes
Oligopeptides
Alanine